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Database: UniProt
Entry: A0A2C9H8T6_ANOQN
LinkDB: A0A2C9H8T6_ANOQN
Original site: A0A2C9H8T6_ANOQN 
ID   A0A2C9H8T6_ANOQN        Unreviewed;      1020 AA.
AC   A0A2C9H8T6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA016895-PA, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA016895-PA}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA016895-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   AlphaFoldDB; A0A2C9H8T6; -.
DR   STRING; 34691.A0A2C9H8T6; -.
DR   EnsemblMetazoa; AQUA016895-RA; AQUA016895-PA; AQUA016895.
DR   VEuPathDB; VectorBase:AQUA016895; -.
DR   Proteomes; UP000076407; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF290; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1020
FT                   /note="Aminopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012699942"
FT   DOMAIN          71..262
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          292..519
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          597..904
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   REGION          954..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        367
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            452
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1020 AA;  113387 MW;  08FEC1617A4E92E8 CRC64;
     MVRSLLLVSL GLCCLLASAD RPPYKSSGIY EEEPQLPGAS DLSGGVASDE IGVAPAQAVD
     ERYRLPTTSI PIHYDLHLRT EIHRNERTFT GTVGIQLQVV QATDKLVMHN RGLVMSSAKV
     SSLPNGVTGA PTLIGDVQYS TDTTFEHITF TSPTILQPGT YLLEVAFQGR LATNDDGFYV
     SSYVADNGER RYLATTQFES TSARMAFPCY DEPGLKATFT VSITHSRSYK AISNMPQKTT
     TDIETDMRTT DFEKTPAMST YLLAFVVSDF LFRVSGTQRV YVRPNAFNEA TFALEAGVKI
     LKVLDDHLGI PYDTYMPKLD QIAIPDFAAG AMENWGLVTY REQALLFNPA VSTYRGKTNV
     ATTIAHEYAH QWFGNLVSPE WWEYIWLNEG FATLYEFYAL DMAYPGQEYW ELFNQQVIQY
     AMGQDGQAST RPMNWNAATP GEISALFDRV AYDKSGSVLN MMRHVLGDDN WKAGLKAYLT
     DRALQGAVDE QLYAGLQSAI EGKGVLPNGV TVSQIMRTWT NEAGYPVLNV RRSYDTGDVI
     ISQERFYNDR KVPNTNIWMI PYNYVHQAKA DFNEFDDFQW LATKAARIET TVPANEWIVF
     NKQQVGYYRV NYDERNWELI TNALHENWAS IHRLNRAQLI DDAYWLARSG RLDLRVALRF
     MTYLRNEREY APWTAANVAL TYFNNRLRGT AEYHNFLVFV DALIEDIYSL LTIDAVSPDD
     TLLHKYLVQT ISTWACSMGY TDCLMKTAAL LKAEASGTGP AVHPDIASVT YCYGMRSALE
     SEFQYLYRKM MNSKNLAERT MLIDSLGCSN NKEFLKAFLT TALGSGTGVE INYRADERRR
     VVQAIYSGGR TGVDALIEFL MDPALVNEFV STLSTSTLNS ALSAIASRTN NVEEMNKLNA
     LITALGSRVN SQTAANLRTT AQANLDWVDG FEGLMLSNFL AEFVAETLST TTAAPETTTV
     TAGPTTTTTT PSSAVTTTTR PTSVTTTVVQ TTTEEDDGAA TIGLSIAALL VSITVHLLMG
//
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